These authors contributed equally to this work.
Probing the Frontiers of Glycoprotein Synthesis: The Fully Elaborated β-Subunit of the Human Follicle-Stimulating Hormone†
Article first published online: 9 DEC 2011
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 51, Issue 4, pages 975–979, January 23, 2012
How to Cite
Nagorny, P., Sane, N., Fasching, B., Aussedat, B. and Danishefsky, S. J. (2012), Probing the Frontiers of Glycoprotein Synthesis: The Fully Elaborated β-Subunit of the Human Follicle-Stimulating Hormone. Angew. Chem. Int. Ed., 51: 975–979. doi: 10.1002/anie.201107482
This work was supported by NIH grant CA103823 (to S.J.D.) and NIH grant CA125934-02 (to P.N.). B.F. is grateful to the Austrian Fonds zur Förderung der wissenschaftlichen Forschung for a fellowship. We thank Rebecca Wilson for assistance with the preparation of the manuscript.
- Issue published online: 17 JAN 2012
- Article first published online: 9 DEC 2011
- Manuscript Received: 24 OCT 2011
- NIH. Grant Number: CA103823
- NIH. Grant Number: CA125934-02
- follicle-stimulating hormone;
- native chemical ligation;
- solid-phase peptide synthesis
Ambitious undertaking: The β-subunit of the human follicle-stimulating hormone (hFSH) displaying a N-linked consensus sequence oligosaccharide at each of the two wild-type sites was synthesized. The glycoprotein has been designed with acetamidomethyl protected cysteine residues, anticipating folding and association with the α-subunit. This represents the largest realistically glycosylated homogeneous glycoprotein obtained by using strictly chemical methods.